Anchoring mechanisms for LFA-3 cell adhesion glycoprotein at membrane surface.
The manner in which a membrane protein is anchored to the lipid bilayer may have a profound influence on its function. Most cell surface membrane proteins are anchored by a membrane-spanning segment(s) of the polypeptide chain, but another type of anchor has been described for several proteins: a ph...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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1987
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| _version_ | 1797056282553745408 |
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| author | Dustin, M Selvaraj, P Mattaliano, R Springer, T |
| author_facet | Dustin, M Selvaraj, P Mattaliano, R Springer, T |
| author_sort | Dustin, M |
| collection | OXFORD |
| description | The manner in which a membrane protein is anchored to the lipid bilayer may have a profound influence on its function. Most cell surface membrane proteins are anchored by a membrane-spanning segment(s) of the polypeptide chain, but another type of anchor has been described for several proteins: a phosphatidyl inositol glycan moiety, attached to the protein C terminus. This type of linkage has been identified on membrane proteins involved in adhesion and transmembrane signalling and could be important in the execution of these functions. We report here that an immunologically important adhesion glycoprotein, lymphocyte function-associated antigen 3 (LFA-3), can be anchored to the membrane by both types of mechanism. These two distinct cell-surface forms of LFA-3 are derived from different biosynthetic precursors. The existence of a phosphatidyl-inositol-linked and a transmembrane anchored form of LFA-3 has important implications for adhesion and transmembrane signalling by LFA-3. |
| first_indexed | 2024-03-06T19:21:11Z |
| format | Journal article |
| id | oxford-uuid:1a246579-c101-44ac-81f4-c428ff042776 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:21:11Z |
| publishDate | 1987 |
| record_format | dspace |
| spelling | oxford-uuid:1a246579-c101-44ac-81f4-c428ff0427762022-03-26T10:53:08ZAnchoring mechanisms for LFA-3 cell adhesion glycoprotein at membrane surface.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:1a246579-c101-44ac-81f4-c428ff042776EnglishSymplectic Elements at Oxford1987Dustin, MSelvaraj, PMattaliano, RSpringer, TThe manner in which a membrane protein is anchored to the lipid bilayer may have a profound influence on its function. Most cell surface membrane proteins are anchored by a membrane-spanning segment(s) of the polypeptide chain, but another type of anchor has been described for several proteins: a phosphatidyl inositol glycan moiety, attached to the protein C terminus. This type of linkage has been identified on membrane proteins involved in adhesion and transmembrane signalling and could be important in the execution of these functions. We report here that an immunologically important adhesion glycoprotein, lymphocyte function-associated antigen 3 (LFA-3), can be anchored to the membrane by both types of mechanism. These two distinct cell-surface forms of LFA-3 are derived from different biosynthetic precursors. The existence of a phosphatidyl-inositol-linked and a transmembrane anchored form of LFA-3 has important implications for adhesion and transmembrane signalling by LFA-3. |
| spellingShingle | Dustin, M Selvaraj, P Mattaliano, R Springer, T Anchoring mechanisms for LFA-3 cell adhesion glycoprotein at membrane surface. |
| title | Anchoring mechanisms for LFA-3 cell adhesion glycoprotein at membrane surface. |
| title_full | Anchoring mechanisms for LFA-3 cell adhesion glycoprotein at membrane surface. |
| title_fullStr | Anchoring mechanisms for LFA-3 cell adhesion glycoprotein at membrane surface. |
| title_full_unstemmed | Anchoring mechanisms for LFA-3 cell adhesion glycoprotein at membrane surface. |
| title_short | Anchoring mechanisms for LFA-3 cell adhesion glycoprotein at membrane surface. |
| title_sort | anchoring mechanisms for lfa 3 cell adhesion glycoprotein at membrane surface |
| work_keys_str_mv | AT dustinm anchoringmechanismsforlfa3celladhesionglycoproteinatmembranesurface AT selvarajp anchoringmechanismsforlfa3celladhesionglycoproteinatmembranesurface AT mattalianor anchoringmechanismsforlfa3celladhesionglycoproteinatmembranesurface AT springert anchoringmechanismsforlfa3celladhesionglycoproteinatmembranesurface |